Mempro™ Cell-Free DNase I-like Protein Production

Based on the comprehensive and excellent membrane protein production platform established through years of experience, scientists from Creative Biostructure can provide first-class custom DNase I-like protein production services through our best Mempro™ cell-free protein expression system for global customers.

Mempro™ cell-free protein production system is the renewed platform developed by Creative Biostructure, which can bypass the limitations that encountered in cell-based protein production system, such as host cell toxicity, low yield and solubilization and purification using detergents, etc.

DNase I-like protein belongs to a protein superfamily that is composed of three families, including endonuclease/exonuclease/phosphatase (EEP) family, arthropod phospholipase D and bacterial phosphatidylinositol-specific phospholipase C. The EEP family can be widely found in endonucleases and phosphatases involved in intracellular signaling. Members of arthropod phospholipase D are actually phospholipases and sphingomyelinases that are identified in a wide range of organisms, such as bacteria, yeast, plants, animals, and viruses. The bacterial phosphatidylinositol-specific phospholipase C are small, water-soluble and calcium-independent enzymes that comprise a single domain folded as a (beta alpha) (8)-barrel. In addition, inositol polyphosphate 5-phosphatase (IPP5) encoded by ITPA gene in humans is one of the members of DNase I-like protein superfamily.

• Mempro™ DNase I-like proteins Production in Rabbit Reticulocyte
Crude rabbit reticulocyte lysate is the innovative system for eukaryotic membrane protein production, providing multiple options for the optimization of the production protocols, such as the availability of materials, protein origin and complexity, downstream processing, etc.

• Mempro™ DNase I-like proteins Production in Baculovirus
Baculovirus expression system from Autographa californica nucleopolyhedrovirus (AcNPV) is also an important host for DNase I-like proteins expression, which is developed in the early stage that transfected insect cells in combination with vectors derived from the baculovirus.